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KMID : 0380219990320060541
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Journal of Biochemistry and Molecular Biology
1999 Volume.32 No. 6 p.541 ~ p.546
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Biochemical Properties of a Chitin-Binding Class III Chitinase in Pumpkin Leaves
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Lee Kyun-Oh
Kim Min-Gab
Jang Ho-Hee
Lee Ji-Yeun
Kim Sun-Chang
Lee Sang-Yeol
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Abstract
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When we compared the chitinase activity of various plant sources using colorimetric or active gel-staining assay methods, the specific activity of pumpkin leaves was the highest among the samples we analyzed. The highly active chitinase from pumpkin leaves (designated PL-ChtIII) was purified to homogeneity using affinity chitin gel and HPLC Mono-Q anion-exchange cloumn chromatographies. In contrast to other members of the class III chitinase family, PL-ChtIII showed a strong binding affinity to the regenerated chitin gel column. The apparent molecular weight of PL-ChtIII was estimated to be 29 kDa on SDS-PAGE gel, while its optimum pH and temperature were shown to be pH 6.0 and 60℃, respectively. Analyzing the reaction products of PL-ChtIII with swollen chitin as substrate, the dimer and tetramer of N-acetylglucosamine were produced as major products in the first hour of the enzymatic reaction along with a small amount of monomers and trimers. As the reaction time increased, dimeric N-acetylglucosamine became the predominant form of reaction product.
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KEYWORD
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Chitin binding activity, Class III chitinase, Enzymatic properties, Pumpkin leaves
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